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• W71372952 endingPage "216" @default.
• W71372952 startingPage "129" @default.
• W71372952 abstract "Information available at present documents the existence of three well-defined classes of guanine nucleotide binding proteins functioning as signal transducers: Gs and Gi which stimulate and inhibit adenylate cyclase, respectively, and transducin which transmits and amplifies the signal from light-activated rhodopsin to cGMP-dependent phosphodiesterase in ROS membranes. Go is a fourth member of this family. Its function is the least known among GTP binding signal transducing proteins. The family of G proteins has a number of properties in common. All are heterotrimers consisting of three subunits, alpha, beta, and gamma. Each of the subunits may be heterogeneous depending on species and tissue of origin and may be posttranslationally modified covalently. The alpha subunits vary in size from 39 to 52 kDa. The sequences for Gs alpha and transducin alpha have 42% overall homology and those of Gi alpha and Gs alpha 43%, whereas those of Gi alpha and transducin alpha have a higher degree (68%) of homology. All alpha subunits bind guanine nucleotides and are ADP-ribosylated by either pertussis toxin (Gi, transducin, Go) or cholera toxin (Gs, Gi, transducin). Thus, transducin and Gi, which have the highest degree of sequence homology, are also ADP-ribosylated by both toxins. The beta subunits have molecular weights of 36 and 35 kDa, respectively. While Gs, Gi, and Go contain a mixture of both, transducin contains only the larger (36-kDa) beta-polypeptide. The relationship of the 36- and the 35-kDa beta subunits is not defined. Although the complete sequence of the 36-kDa beta subunit of transducin has been deduced from the cDNA sequence, complete sequences of other beta subunits are not yet available so that detailed comparisons cannot be made at present. However, the proteolytic profiles of each class of the beta subunits of different G proteins are indistinguishable. The gamma subunit of bovine transducin has been completely sequenced. It has a Mr of 8400. Again complete sequences of other gamma subunits are not yet available. While the gamma subunits of Gs, Gi, and Go have identical electrophoretic mobility in SDS gels, they differ significantly in this respect from the gamma subunit of transducin. Moreover, crossover experiments point to functional differences between gamma subunits from G protein and transducin complexes. In addition, a role for beta, gamma in anchoring guanine nucleotide binding proteins to membranes has been postulated.(ABSTRACT TRUNCATED AT 400 WORDS)" @default.
• W71372952 created "2016-06-24" @default.
• W71372952 creator A5008211775 @default.
• W71372952 creator A5082635329 @default.
• W71372952 date "1988-01-01" @default.
• W71372952 modified "2023-10-13" @default.
• W71372952 title "Structural and Functional Relationships of Guanosine Triphosphate Binding Proteins" @default.
• W71372952 cites W111440207 @default.
• W71372952 cites W124504601 @default.
• W71372952 cites W1480125182 @default.
• W71372952 cites W1481499718 @default.
• W71372952 cites W1484188159 @default.
• W71372952 cites W1485278468 @default.
• W71372952 cites W1490249812 @default.
• W71372952 cites W1490796893 @default.
• W71372952 cites W1490808252 @default.
• W71372952 cites W1494455361 @default.
• W71372952 cites W1496654715 @default.
• W71372952 cites W1496864275 @default.
• W71372952 cites W1498034410 @default.
• W71372952 cites W1498162448 @default.
• W71372952 cites W1499138436 @default.
• W71372952 cites W1501934404 @default.
• W71372952 cites W1503279779 @default.
• W71372952 cites W1503509391 @default.
• W71372952 cites W1505544453 @default.
• W71372952 cites W1507560840 @default.
• W71372952 cites W1508955850 @default.
• W71372952 cites W1509164711 @default.
• W71372952 cites W1510671746 @default.
• W71372952 cites W1511336559 @default.
• W71372952 cites W1511887721 @default.
• W71372952 cites W1513905140 @default.
• W71372952 cites W1521095349 @default.
• W71372952 cites W1525223486 @default.
• W71372952 cites W1528087101 @default.
• W71372952 cites W1531504909 @default.
• W71372952 cites W1532747508 @default.
• W71372952 cites W1533101741 @default.
• W71372952 cites W1533887373 @default.
• W71372952 cites W1535671912 @default.
• W71372952 cites W1535986268 @default.
• W71372952 cites W1539001739 @default.
• W71372952 cites W1543217424 @default.
• W71372952 cites W1543525864 @default.
• W71372952 cites W1543967583 @default.
• W71372952 cites W1544086249 @default.
• W71372952 cites W1545162664 @default.
• W71372952 cites W1545247716 @default.
• W71372952 cites W1547271459 @default.
• W71372952 cites W1550019326 @default.
• W71372952 cites W1551266724 @default.
• W71372952 cites W1551274638 @default.
• W71372952 cites W1553656232 @default.
• W71372952 cites W1553818986 @default.
• W71372952 cites W1561254531 @default.
• W71372952 cites W1562025403 @default.
• W71372952 cites W1562998862 @default.
• W71372952 cites W1563418303 @default.
• W71372952 cites W1563931720 @default.
• W71372952 cites W1564457890 @default.
• W71372952 cites W1565515078 @default.
• W71372952 cites W1565707912 @default.
• W71372952 cites W1566050966 @default.
• W71372952 cites W1566146794 @default.
• W71372952 cites W1567325248 @default.
• W71372952 cites W1568437007 @default.
• W71372952 cites W1569033208 @default.
• W71372952 cites W1570762629 @default.
• W71372952 cites W1570939625 @default.
• W71372952 cites W1571926774 @default.
• W71372952 cites W1573718340 @default.
• W71372952 cites W1573946811 @default.
• W71372952 cites W1577436652 @default.
• W71372952 cites W1577885145 @default.
• W71372952 cites W1586632187 @default.
• W71372952 cites W1595771065 @default.
• W71372952 cites W1597332117 @default.
• W71372952 cites W1601839528 @default.
• W71372952 cites W1602129277 @default.
• W71372952 cites W1603066709 @default.
• W71372952 cites W1615152444 @default.
• W71372952 cites W1649341288 @default.
• W71372952 cites W1652720512 @default.
• W71372952 cites W1653242653 @default.
• W71372952 cites W1653853239 @default.
• W71372952 cites W1658992953 @default.
• W71372952 cites W1662790201 @default.
• W71372952 cites W1676716323 @default.
• W71372952 cites W1745921889 @default.
• W71372952 cites W1802073588 @default.
• W71372952 cites W1863678882 @default.
• W71372952 cites W1895492779 @default.
• W71372952 cites W1912130517 @default.
• W71372952 cites W1926371675 @default.
• W71372952 cites W1963704405 @default.
• W71372952 cites W1964585383 @default.
• W71372952 cites W1965058394 @default.

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